Population of ATP synthase molecules in mitochondria is limited by available 6.8-kDa proteolipid protein (MLQ)

Genes Cells. 2014 Feb;19(2):153-60. doi: 10.1111/gtc.12121. Epub 2013 Dec 13.

Abstract

A 6.8-kDa proteolipid (called MLQ) is a hydrophobic mitochondrial protein with unknown function that is loosely associated with ATP synthase. Here, we show that MLQ-knockdown HeLa cells lose population of ATP synthase in mitochondria. This is not due to low transcription of subunit genes of ATP synthase because levels of mRNA for α- and β-subunits are unaffected by the knockdown. As a consequence, the knockdown cells show low mitochondrial ATP synthesis activity, grow slowly in the normal medium, and are vulnerable to glucose deprivation. Given that the expression of MLQ varies responding to cellular conditions, MLQ is a potential regulator of the mitochondrial ATP synthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Enlargement
  • Cell Survival
  • Electron Transport Chain Complex Proteins / metabolism
  • HeLa Cells
  • Humans
  • Membrane Potential, Mitochondrial
  • Mitochondria / genetics
  • Mitochondria / metabolism*
  • Mitochondrial Proteins / genetics
  • Mitochondrial Proteins / metabolism*
  • Mitochondrial Proton-Translocating ATPases
  • Proteolipids / genetics
  • Proteolipids / metabolism*
  • Proton-Translocating ATPases / genetics
  • Proton-Translocating ATPases / metabolism*
  • RNA, Messenger / metabolism

Substances

  • ATP5MJ protein, human
  • Electron Transport Chain Complex Proteins
  • Mitochondrial Proteins
  • Proteolipids
  • RNA, Messenger
  • Mitochondrial Proton-Translocating ATPases
  • Proton-Translocating ATPases